Analytical Data
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Gene name
CUL5-RBX2
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简介
The CUL5 protein is a core component of the SCF-like ECS E3 ubiquitin-protein ligase complex. CUL5/RBX2 Protein, Human (Active, Sf9, His, Strep) is the recombinant human-derived CUL5/RBX2, expressed by Sf9 insect cells, with Strep, His labeled tag.
- Application
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Alternative Names
VACM1
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Species
Human
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Source
Baculovirus
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Tag
N-StrepⅡ;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q93034 (A2-A780)&Q9UBF6
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Expression Region
Q93034 (A2-A780)&Q9UBF6 (A2-K113)
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
CUL5-RBX2 is a crucial component of the E3 ubiquitin ligase complex, which plays a significant role in the ubiquitination process, a post-translational modification that regulates protein stability, localization, and function. The CUL5 (Cullin 5) protein acts as a scaffold, connecting a variety of substrate recognition molecules, while RBX2 (RING-box 2) serves as the RING finger protein that facilitates the transfer of ubiquitin moieties to target substrates. This complex is integral in controlling numerous cellular processes, including cell cycle regulation, signal transduction, and immune responses. Disruptions in the function of CUL5-RBX2 have been implicated in various diseases, including cancer, where aberrant ubiquitination can lead to uncontrolled cell growth and tumorigenesis. Recent studies have focused on elucidating the structural and functional dynamics of CUL5-RBX2, as well as its interactions with substrate proteins and other regulatory components. Understanding the mechanisms by which CUL5-RBX2 mediates ubiquitination can provide insights into disease mechanisms and may uncover potential therapeutic targets for intervention. Researchers are employing advanced biophysical techniques and cellular models to explore the complexity of this ligase complex, highlighting its significance in maintaining cellular homeostasis and its potential as a target for drug development in malignancies where ubiquitination pathways are altered. Overall, the study of CUL5-RBX2 is vital for comprehending the intricate regulation of protein turnover in the cell and its implications in health and disease.
